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Q9X844 (PANC_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantothenate synthetase

Short name=PS
EC=6.3.2.1
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene names
Name:panC
Ordered Locus Names:SCO3383
ORF Names:SCE126.01c, SCE94.34c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. HAMAP-Rule MF_00158

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00158

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity.

Sequence similarities

Belongs to the pantothenate synthetase family.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantoate-beta-alanine ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128278

Regions

Nucleotide binding31 – 388ATP By similarity
Nucleotide binding152 – 1554ATP By similarity
Nucleotide binding189 – 1924ATP By similarity

Sites

Active site381Proton donor By similarity
Binding site651Beta-alanine By similarity
Binding site651Pantoate By similarity
Binding site1581Pantoate By similarity
Binding site1811ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9X844 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 3C948F7014A2913C

FASTA33735,456
        10         20         30         40         50         60 
MTTPTPPVLL RTAGELHARV RRGRRAVVMT MGALHEGHAT LIRTARDIAG PDGEVVVTVF 

        70         80         90        100        110        120 
VNPLQFGAGE DLDRYPRTLD ADLEIAGRAG ADAVFAPAVD EVYPGGEPQV RVTAGPMGGR 

       130        140        150        160        170        180 
LEGASRPGHF DGMLTVVAKL LHLTRPDLAL YGQKDAQQLA LIRRMVRDLN FGVEIVGVPT 

       190        200        210        220        230        240 
VREEDGLALS SRNRYLSTAE RRTALALSQA LFAGLDRHAA QEALCARARE VPATQARAEA 

       250        260        270        280        290        300 
LSALGESRAA ADAHAVATSA PGSATAVRDA ARLVLDDAAR ATPPLELDYL ALVDPSDFTE 

       310        320        330 
IGDDHTGEAV LAVAARVGAT RLIDNVHLTF GPLGAAS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939116 Genomic DNA. Translation: CAD55315.1.
RefSeqNP_733602.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9X844.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO3383.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD55315; CAD55315; CAD55315.
GeneID1098820.
KEGGsco:SCO3383.
PATRIC23736522. VBIStrCoe124346_3446.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAGGEPQVR.
OrthoDBEOG6Z6FZ4.
PhylomeDBQ9X844.
ProtClustDBPRK00380.

Enzyme and pathway databases

UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 2 hits.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_STRCO
AccessionPrimary (citable) accession number: Q9X844
Secondary accession number(s): Q9X8N9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways